ID   GPX3_MOUSE              Reviewed;         226 AA.
AC   P46412; Q5XKR0;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-NOV-2009, entry version 86.
DE   RecName: Full=Glutathione peroxidase 3;
DE            EC=1.11.1.9;
DE   AltName: Full=GSHPx-3;
DE            Short=GPx-3;
DE   AltName: Full=Plasma glutathione peroxidase;
DE   AltName: Full=GSHPx-P;
DE   Flags: Precursor;
GN   Name=Gpx3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=95014577; PubMed=7929449;
RA   Maser R.L., Magenheimer B.S., Calvet J.P.;
RT   "Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal
RT   proximal tubular expression and secretion.";
RL   J. Biol. Chem. 269:27066-27073(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and NMRI; TISSUE=Colon, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX   PubMed=8566787; DOI=10.1016/0378-1119(95)00551-X;
RA   Schwaab V., Baud E., Ghyselinck N.B., Mattei M.-G., Dufaure J.-P.,
RA   Drevet J.R.;
RT   "Cloning of the mouse gene encoding plasma glutathione peroxidase:
RT   organization, sequence and chromosomal localization.";
RL   Gene 167:25-31(1995).
CC   -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC       catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC       organic hydroperoxide, by glutathione.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Secreted in plasma.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; U13705; AAA62283.2; -; mRNA.
DR   EMBL; AK002219; BAC55243.1; -; mRNA.
DR   EMBL; AK004942; BAC55250.1; -; mRNA.
DR   EMBL; AK146760; BAE27413.1; -; mRNA.
DR   EMBL; BC003339; AAH03339.1; -; mRNA.
DR   EMBL; BC037027; AAH37027.1; -; mRNA.
DR   EMBL; BC049235; AAH49235.1; -; mRNA.
DR   EMBL; BC061950; AAH61950.1; -; mRNA.
DR   EMBL; X84742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00133536; -.
DR   PIR; A55086; A55086.
DR   RefSeq; NP_001077398.1; -.
DR   RefSeq; NP_032187.2; -.
DR   UniGene; Mm.200916; -.
DR   HSSP; P00435; 1GP1.
DR   STRING; P46412; -.
DR   PeroxiBase; 3711; MmGPx03.
DR   PRIDE; P46412; -.
DR   Ensembl; ENSMUST00000082430; ENSMUSP00000081011; ENSMUSG00000018339; Mus musculus.
DR   GeneID; 14778; -.
DR   KEGG; mmu:14778; -.
DR   CTD; 14778; -.
DR   MGI; MGI:105102; Gpx3.
DR   HOGENOM; P46412; -.
DR   HOVERGEN; P46412; -.
DR   OMA; YMRRQAA; -.
DR   BRENDA; 1.11.1.9; 244.
DR   NextBio; 286887; -.
DR   ArrayExpress; P46412; -.
DR   Bgee; P46412; -.
DR   CleanEx; MM_GPX3; -.
DR   Genevestigator; P46412; -.
DR   GermOnline; ENSMUSG00000018339; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0008430; F:selenium binding; ISS:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Peroxidase; Secreted; Selenium; Selenocysteine;
KW   Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    226       Glutathione peroxidase 3.
FT                                /FTId=PRO_0000013063.
FT   ACT_SITE     73     73
FT   NON_STD      73     73       Selenocysteine.
FT   CONFLICT      6      7       RA -> Q (in Ref. 4).
FT   CONFLICT     21     21       P -> A (in Ref. 4).
FT   CONFLICT     24     29       GQEKSK -> DKRSLR (in Ref. 4).
SQ   SEQUENCE   226 AA;  25424 MW;  D9706574929E3F86 CRC64;
     MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG EEYIPFKQYA
     GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP SNQFGKQEPG ENSEILPSLK
     YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR
     WNFEKFLVGP DGIPVMRWYH RTTVSNVKMD ILSYMRRQAA LSARGK
//